EFNA5_CHICK
ID EFNA5_CHICK Reviewed; 228 AA.
AC P52804;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Ephrin-A5;
DE AltName: Full=EPH-related receptor tyrosine kinase ligand 7;
DE Short=LERK-7;
DE AltName: Full=Repulsive axon guidance signal protein;
DE Flags: Precursor;
GN Name=EFNA5; Synonyms=RAGS;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Posterior tectum;
RX PubMed=7634326; DOI=10.1016/0092-8674(95)90425-5;
RA Drescher U., Kremoser C., Handwerker C., Loschinger J., Noda M.,
RA Bonhoeffer F.;
RT "In vitro guidance of retinal ganglion cell axons by RAGS, a 25 kDa tectal
RT protein related to ligands for Eph receptor tyrosine kinases.";
RL Cell 82:359-370(1995).
CC -!- FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of
CC receptor tyrosine kinases which are crucial for migration, repulsion
CC and adhesion during neuronal, vascular and epithelial development.
CC Binds promiscuously Eph receptors residing on adjacent cells, leading
CC to contact-dependent bidirectional signaling into neighboring cells.
CC Induces compartmentalized signaling within a caveolae-like membrane
CC microdomain when bound to the extracellular domain of its cognate
CC receptor. This signaling event requires the activity of the Fyn
CC tyrosine kinase. Activates the EPHA3 receptor to regulate cell-cell
CC adhesion and cytoskeletal organization. With the receptor EPHA2 may
CC regulate lens fiber cells shape and interactions and be important for
CC lens transparency maintenance. May function actively to stimulate axon
CC fasciculation (By similarity). Induces growth cone collapse and
CC repulsion of retinal ganglion cell axons. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in a graded fashion across the tectum
CC being more strongly expressed towards the posterior pole.
CC -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00884}.
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DR EMBL; X90377; CAA62027.1; -; mRNA.
DR PIR; A57084; A57084.
DR RefSeq; NP_990515.1; NM_205184.2.
DR AlphaFoldDB; P52804; -.
DR SMR; P52804; -.
DR STRING; 9031.ENSGALP00000000368; -.
DR PaxDb; P52804; -.
DR GeneID; 396100; -.
DR KEGG; gga:396100; -.
DR CTD; 1946; -.
DR VEuPathDB; HostDB:geneid_396100; -.
DR eggNOG; KOG3858; Eukaryota.
DR InParanoid; P52804; -.
DR OrthoDB; 1094764at2759; -.
DR PhylomeDB; P52804; -.
DR PRO; PR:P52804; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045499; F:chemorepellent activity; ISS:AgBase.
DR GO; GO:0046875; F:ephrin receptor binding; ISS:AgBase.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; ISS:AgBase.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; ISS:AgBase.
DR CDD; cd10425; Ephrin-A_Ectodomain; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR031328; Ephrin.
DR InterPro; IPR034252; Ephrin-A_Ecto.
DR InterPro; IPR019765; Ephrin_CS.
DR InterPro; IPR001799; Ephrin_RBD.
DR PANTHER; PTHR11304; PTHR11304; 1.
DR Pfam; PF00812; Ephrin; 1.
DR PRINTS; PR01347; EPHRIN.
DR SUPFAM; SSF49503; SSF49503; 1.
DR PROSITE; PS01299; EPHRIN_RBD_1; 1.
DR PROSITE; PS51551; EPHRIN_RBD_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Neurogenesis;
KW Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..203
FT /note="Ephrin-A5"
FT /id="PRO_0000008383"
FT PROPEP 204..228
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000008384"
FT DOMAIN 29..162
FT /note="Ephrin RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT LIPID 203
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT DISULFID 90..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
SQ SEQUENCE 228 AA; 26206 MW; 56D8E4FBDECF18AD CRC64;
MPHVEMLLLA VAALWVCVRG QEPGRKAVAD RYAVYWNSTN PRFQQGDYHI DVCINDYLDV
FCPHYEDSVP EDKTERYVLY MVNFDGYSSC DHISKGFKRW ECNRPHSPNG PLKFSEKFQL
FTPFSLGFEF RPGREYFYIS SAIPDNGRRS CLKLKVFVRP ANSCMKTIGV HDRVFDVNDK
VENSLEPADD TVRESAEPSR GENAAQTPRI PIRLLATLLF LLAMLLIL
